Synthesis of Bacillus cereus spore coat protein.
The major structural protein of Bacillus cereus spore coats was synthesized, commencing 1 to 2 h after the end of exponential growth, as a precursor with a mass of ca. 65,000 daltons. About 40% of this precursor, i.e. 26,000 daltons, was converted to spore coat monomers of 13,000 daltons each, perhaps as disulfide-linked dimers. The rate of conversion varied, being initially slow, most rapid at the time of morphogenesis of the coat layers, and then slow again late in sporulation, coincident with a decrease in intracellular protease activity. There was a second major spore coat polypeptide of about 26,000 daltons that was extractable from mature spores in variable amounts. This protein had a peptide profile and a reactivity with spore coat protein antibody that were very similar to those of the 13,000-dalton monomers. It is probably a disulfide-linked dimer that is not readily dissociated.
D001409:Bacillus cereus / Q000502:physiology*; D001426:Bacterial Proteins / Q000096:biosynthesis*; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D011498:Protein Precursors / Q000096:biosynthesis*; D013171:Spores, Bacterial / Q000378:metabolism
D001426:Bacterial Proteins; D011498:Protein Precursors; D010447:Peptide Hydrolases